Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24]

 MMP24_HUMAN             Reviewed;         645 AA.
Q9Y5R2; B7ZBG8; Q9H440;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 170.
RecName: Full=Matrix metalloproteinase-24;
Short=MMP-24;
EC=3.4.24.-;
AltName: Full=Membrane-type matrix metalloproteinase 5;
Short=MT-MMP 5;
Short=MTMMP5;
AltName: Full=Membrane-type-5 matrix metalloproteinase;
Short=MT5-MMP;
Short=MT5MMP;
Contains:
RecName: Full=Processed matrix metalloproteinase-24;
Flags: Precursor;
Name=MMP24; Synonyms=MT5MMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10363975;
Llano E., Pendas A.M., Freije J.P., Nakano A., Knaeuper V., Murphy G.,
Lopez-Otin C.;
"Identification and characterization of human MT5-MMP, a new membrane-
bound activator of progelatinase a overexpressed in brain tumors.";
Cancer Res. 59:2570-2576(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Seiki M.;
"Identification of a new membrane-type matrix metalloproteinase, MT5-
MMP, that is expressed predominantly in cerebellum.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
-!- FUNCTION: Metalloprotease that mediates cleavage of N-cadherin
(CDH2) and acts as a regulator of neuro-immune interactions and
neural stem cell quiescence. Involved in cell-cell interactions
between nociceptive neurites and mast cells, possibly by mediating
cleavage of CDH2, thereby acting as a mediator of peripheral
thermal nociception and inflammatory hyperalgesia. Key regulator
of neural stem cells quiescence by mediating cleavage of CDH2,
affecting CDH2-mediated anchorage of neural stem cells to
ependymocytes in the adult subependymal zone, leading to modulate
their quiescence. May play a role in axonal growth. Able to
activate progelatinase A. May also be a proteoglycanase involved
in degradation of proteoglycans, such as dermatan sulfate and
chondroitin sulfate proteoglycans. Cleaves partially fibronectin,
but not collagen type I, nor laminin (By similarity).
{ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts (via PDZ-binding motif) with APBA3 (via PDZ
domain). Interacts with GRIP1 and GRIP2 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Matrix metalloproteinase-24: Cell membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Golgi apparatus, trans-Golgi network membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}. Note=Recycled
back to the plasma membrane through the trans-Golgi network via
interaction with APBA3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed matrix metalloproteinase-24:
Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Note=Also shed from cell surface as soluble proteinase, by a
proteolytic cleavage. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Predominantly expressed in brain, kidney,
pancreas and lung. Overexpressed in a series of brain tumors,
including astrocytomas and glioblastomas.
{ECO:0000269|PubMed:10363975}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- DOMAIN: The PDZ-binding motif (also named EWV motif) is required
for interaction with PDZ domains of APBA3 and recycling through
the trans-Golgi network. {ECO:0000250}.
-!- PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF131284; AAD42962.1; -; mRNA.
EMBL; AB021227; BAA82967.1; -; mRNA.
EMBL; AL121753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS46593.1; -.
RefSeq; NP_006681.1; NM_006690.3.
UniGene; Hs.715494; -.
ProteinModelPortal; Q9Y5R2; -.
SMR; Q9Y5R2; -.
IntAct; Q9Y5R2; 1.
MINT; Q9Y5R2; -.
STRING; 9606.ENSP00000246186; -.
BindingDB; Q9Y5R2; -.
ChEMBL; CHEMBL5050; -.
DrugBank; DB00786; Marimastat.
MEROPS; M10.023; -.
iPTMnet; Q9Y5R2; -.
PhosphoSitePlus; Q9Y5R2; -.
BioMuta; MMP24; -.
DMDM; 12585280; -.
EPD; Q9Y5R2; -.
MaxQB; Q9Y5R2; -.
PaxDb; Q9Y5R2; -.
PeptideAtlas; Q9Y5R2; -.
PRIDE; Q9Y5R2; -.
ProteomicsDB; 86480; -.
DNASU; 10893; -.
Ensembl; ENST00000246186; ENSP00000246186; ENSG00000125966.
GeneID; 10893; -.
KEGG; hsa:10893; -.
UCSC; uc002xbu.3; human.
CTD; 10893; -.
DisGeNET; 10893; -.
EuPathDB; HostDB:ENSG00000125966.9; -.
GeneCards; MMP24; -.
HGNC; HGNC:7172; MMP24.
HPA; HPA049280; -.
MIM; 604871; gene.
neXtProt; NX_Q9Y5R2; -.
OpenTargets; ENSG00000125966; -.
PharmGKB; PA30881; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9Y5R2; -.
KO; K08002; -.
OMA; FQFKNKA; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q9Y5R2; -.
TreeFam; TF352396; -.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
ChiTaRS; MMP24; human.
GeneWiki; MMP24; -.
GenomeRNAi; 10893; -.
PRO; PR:Q9Y5R2; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125966; Expressed in 159 organ(s), highest expression level in right hemisphere of cerebellum.
CleanEx; HS_MMP24; -.
Genevisible; Q9Y5R2; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISS:UniProtKB.
GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028723; MMP24.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF138; PTHR10201:SF138; 1.
Pfam; PF11857; DUF3377; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Golgi apparatus; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 52 {ECO:0000255}.
PROPEP 53 155 {ECO:0000250}.
/FTId=PRO_0000028846.
CHAIN 156 645 Matrix metalloproteinase-24.
/FTId=PRO_0000028847.
CHAIN 156 581 Processed matrix metalloproteinase-24.
{ECO:0000250}.
/FTId=PRO_0000302758.
TOPO_DOM 53 602 Extracellular. {ECO:0000255}.
TRANSMEM 603 623 Helical. {ECO:0000255}.
TOPO_DOM 624 645 Cytoplasmic. {ECO:0000255}.
REPEAT 377 425 Hemopexin 1.
REPEAT 426 471 Hemopexin 2.
REPEAT 473 521 Hemopexin 3.
REPEAT 522 569 Hemopexin 4.
MOTIF 137 144 Cysteine switch. {ECO:0000250}.
MOTIF 643 645 PDZ-binding.
COMPBIAS 149 152 Poly-Arg.
ACT_SITE 283 283 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 139 139 Zinc; in inhibited form. {ECO:0000250}.
METAL 282 282 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 286 286 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 292 292 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
SITE 581 582 Cleavage; by furin. {ECO:0000250}.
DISULFID 380 569 {ECO:0000250}.
VARIANT 564 564 R -> H (in dbSNP:rs751887).
/FTId=VAR_060166.
SEQUENCE 645 AA; 73231 MW; 06B2B76EA3DABB9D CRC64;
MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA RAAAAAAGAG
NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA LHSAKALQSA VSTMQQFYGI
PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR RRNKRYALTG QKWRQKHITY SIHNYTPKVG
ELDTRKAIRQ AFDVWQKVTP LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG
FLAHAYFPGP GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM
APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP SERKHERQPR
PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR WFWRLRNNRV QEGYPMQIEQ
FWKGLPARID AAYERADGRF VFFKGDKYWV FKEVTVEPGY PHSLGELGSC LPREGIDTAL
RWEPVGKTYF FKGERYWRYS EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK
GRDYWKFDNQ KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV
NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV


Related products :

Catalog number Product name Quantity
E0555h ELISA Homo sapiens,Human,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,MMP24,MMP-24,MT5MMP,MT5MMP,MT5-MMP,MT-MMP 5,MTMMP5 96T
U0555h CLIA Homo sapiens,Human,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,MMP24,MMP-24,MT5MMP,MT5MMP,MT5-MMP,MT-MMP 5,MTMMP5 96T
E0555h ELISA kit Homo sapiens,Human,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,MMP24,MMP-24,MT5MMP,MT5MMP,MT5-MMP,MT-MMP 5,MTMMP5 96T
E0555r ELISA kit Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp24,MMP-24,MT5MMP,Mt5mmp,MT5-MMP,MT-MMP 5,MTMMP5,Rat,Rattus norvegicus 96T
E0555r ELISA Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp24,MMP-24,MT5MMP,Mt5mmp,MT5-MMP,MT-MMP 5,MTMMP5,Rat,Rattus norvegicus 96T
U0555r CLIA Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp24,MMP-24,MT5MMP,Mt5mmp,MT5-MMP,MT-MMP 5,MTMMP5,Rat,Rattus norvegicus 96T
E0555m ELISA Matrix metalloproteinase-21,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp21,MMP-21,Mmp24,MMP-24,Mouse,MT5MMP,Mt5mmp,MT5-MMP,MT 96T
U0555m CLIA Matrix metalloproteinase-21,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp21,MMP-21,Mmp24,MMP-24,Mouse,MT5MMP,Mt5mmp,MT5-MMP,MT- 96T
E0555m ELISA kit Matrix metalloproteinase-21,Matrix metalloproteinase-24,Membrane-type matrix metalloproteinase 5,Membrane-type-5 matrix metalloproteinase,Mmp21,MMP-21,Mmp24,MMP-24,Mouse,MT5MMP,Mt5mmp,MT5-M 96T
U2056h CLIA kit Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056m ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus muscu 96T
E2056h ELISA Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056h ELISA kit Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056r ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Rat,Rattus norvegicus 96T
U2056r CLIA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Rat,Rattus norvegicus 96T
U2056Rb CLIA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Oryctolagus cuniculus,Rabbit 96T
E2056r ELISA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Rat,Rattus norvegicus 96T
E2056Rb ELISA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Oryctolagus cuniculus,Rabbit 96T
E2056m ELISA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus musculus 96T
U2056m CLIA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus muscul 96T
U2056m CLIA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus musculus 96T
E2056Rb ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Oryctolagus cuniculus,Rabbit 96T
U2056r CLIA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Rat,Rattus norvegicus 96T
U2056h CLIA Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
U2056Rb CLIA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Oryctolagus cuniculus,Rabbit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur